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SWI3B_ARATH
ID   SWI3B_ARATH             Reviewed;         469 AA.
AC   Q84JG2; O22811;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=SWI/SNF complex subunit SWI3B;
DE            Short=AtSWI3B;
DE   AltName: Full=Transcription regulatory protein SWI3B;
GN   Name=SWI3B; Synonyms=CHB2; OrderedLocusNames=At2g33610; ORFNames=F4P9.38;
OS   Arabidopsis thaliana (Mouse-ear cress).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX   NCBI_TaxID=3702;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DISRUPTION PHENOTYPE, TISSUE
RP   SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH SWI3A; SWI3C; SWI3D;
RP   BSH AND FCA, AND SUBUNIT.
RX   PubMed=16055636; DOI=10.1105/tpc.105.031203;
RA   Sarnowski T.J., Rios G., Jasik J., Swiezewski S., Kaczanowski S., Li Y.,
RA   Kwiatkowska A., Pawlikowska K., Kozbial M., Kozbial P., Koncz C.,
RA   Jerzmanowski A.;
RT   "SWI3 subunits of putative SWI/SNF chromatin-remodeling complexes play
RT   distinct roles during Arabidopsis development.";
RL   Plant Cell 17:2454-2472(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=10617197; DOI=10.1038/45471;
RA   Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA   Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA   Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA   Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA   Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA   Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA   Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT   "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL   Nature 402:761-768(1999).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Columbia;
RX   PubMed=27862469; DOI=10.1111/tpj.13415;
RA   Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA   Town C.D.;
RT   "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT   genome.";
RL   Plant J. 89:789-804(2017).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Columbia;
RX   PubMed=14593172; DOI=10.1126/science.1088305;
RA   Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA   Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA   Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA   Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA   Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA   Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA   Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA   Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA   Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA   Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA   Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA   Ecker J.R.;
RT   "Empirical analysis of transcriptional activity in the Arabidopsis
RT   genome.";
RL   Science 302:842-846(2003).
RN   [5]
RP   FUNCTION, INTERACTION WITH SWI3A; SWI3C; BSH AND FCA, AND SUBUNIT.
RX   PubMed=12140326; DOI=10.1093/nar/gkf458;
RA   Sarnowski T.J., Swiezewski S., Pawlikowska K., Kaczanowski S.,
RA   Jerzmanowski A.;
RT   "AtSWI3B, an Arabidopsis homolog of SWI3, a core subunit of yeast Swi/Snf
RT   chromatin remodeling complex, interacts with FCA, a regulator of flowering
RT   time.";
RL   Nucleic Acids Res. 30:3412-3421(2002).
RN   [6]
RP   FUNCTION, AND TISSUE SPECIFICITY.
RX   PubMed=14682613; DOI=10.1023/b:plan.0000004305.60407.8b;
RA   Zhou C., Miki B., Wu K.;
RT   "CHB2, a member of the SWI3 gene family, is a global regulator in
RT   Arabidopsis.";
RL   Plant Mol. Biol. 52:1125-1134(2003).
RN   [7]
RP   INTERACTION WITH BRM.
RX   PubMed=16845477; DOI=10.1007/s11103-006-9021-2;
RA   Hurtado L., Farrona S., Reyes J.C.;
RT   "The putative SWI/SNF complex subunit BRAHMA activates flower homeotic
RT   genes in Arabidopsis thaliana.";
RL   Plant Mol. Biol. 62:291-304(2006).
RN   [8]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH HAB1.
RX   PubMed=19033529; DOI=10.1105/tpc.107.056705;
RA   Saez A., Rodrigues A., Santiago J., Rubio S., Rodriguez P.L.;
RT   "HAB1-SWI3B interaction reveals a link between abscisic acid signaling and
RT   putative SWI/SNF chromatin-remodeling complexes in Arabidopsis.";
RL   Plant Cell 20:2972-2988(2008).
RN   [9]
RP   INTERACTION WITH MORC6 AND SUVH9.
RX   PubMed=27171427; DOI=10.1371/journal.pgen.1006026;
RA   Liu Z.-W., Zhou J.-X., Huang H.-W., Li Y.-Q., Shao C.-R., Li L., Cai T.,
RA   Chen S., He X.-J.;
RT   "Two components of the RNA-Directed DNA methylation pathway associate with
RT   MORC6 and silence loci targeted by MORC6 in Arabidopsis.";
RL   PLoS Genet. 12:E1006026-E1006026(2016).
CC   -!- FUNCTION: Component of a multiprotein complex equivalent of the SWI/SNF
CC       complex, an ATP-dependent chromatin-remodeling complex, which is
CC       required for the positive and negative regulation of gene expression of
CC       a large number of genes. It changes chromatin structure by altering
CC       DNA-histone contacts within a nucleosome, leading eventually to a
CC       change in nucleosome position, thus facilitating or repressing binding
CC       of gene-specific transcription factors. May play an essential role in
CC       the transition from the vegetative to the reproductive phase of
CC       development. May be a positive regulator of ABA signaling.
CC       {ECO:0000269|PubMed:12140326, ECO:0000269|PubMed:14682613,
CC       ECO:0000269|PubMed:16055636, ECO:0000269|PubMed:19033529}.
CC   -!- SUBUNIT: Homodimers and heterodimers. Interacts with SWI3A, SWI3C,
CC       SWI3D, BSH, BRM and FCA (via C-terminus), and (via N-terminus) with
CC       HAB1. Interacts with MORC6 and SUVH9 (PubMed:27171427).
CC       {ECO:0000269|PubMed:12140326, ECO:0000269|PubMed:16055636,
CC       ECO:0000269|PubMed:16845477, ECO:0000269|PubMed:19033529,
CC       ECO:0000269|PubMed:27171427}.
CC   -!- INTERACTION:
CC       Q84JG2; O04719: ABI2; NbExp=2; IntAct=EBI-1102271, EBI-537680;
CC       Q84JG2; Q9ASZ1: GEBP; NbExp=3; IntAct=EBI-1102271, EBI-15191723;
CC       Q84JG2; Q8VYD2: GPL1; NbExp=3; IntAct=EBI-1102271, EBI-4426914;
CC       Q84JG2; Q9CAJ0: HAB1; NbExp=4; IntAct=EBI-1102271, EBI-2309302;
CC       Q84JG2; P46639: KNAT1; NbExp=6; IntAct=EBI-1102271, EBI-530486;
CC       Q84JG2; Q9XI07: SWI3C; NbExp=4; IntAct=EBI-1102271, EBI-1102300;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00624,
CC       ECO:0000269|PubMed:16055636, ECO:0000269|PubMed:19033529}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, stems, leaves, flowers and
CC       siliques. {ECO:0000269|PubMed:14682613, ECO:0000269|PubMed:16055636}.
CC   -!- DISRUPTION PHENOTYPE: Plants have pleiotropic developmental
CC       abnormalities including embryo development blocked at the early
CC       globular stage. {ECO:0000269|PubMed:16055636}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB80676.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AC002332; AAB80676.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; CP002685; AEC08859.1; -; Genomic_DNA.
DR   EMBL; BT004085; AAO42112.1; -; mRNA.
DR   EMBL; BT005094; AAO50627.1; -; mRNA.
DR   PIR; F84747; F84747.
DR   RefSeq; NP_180919.2; NM_128921.6.
DR   AlphaFoldDB; Q84JG2; -.
DR   SMR; Q84JG2; -.
DR   BioGRID; 3274; 152.
DR   IntAct; Q84JG2; 28.
DR   STRING; 3702.AT2G33610.1; -.
DR   iPTMnet; Q84JG2; -.
DR   PaxDb; Q84JG2; -.
DR   PRIDE; Q84JG2; -.
DR   ProteomicsDB; 226798; -.
DR   EnsemblPlants; AT2G33610.1; AT2G33610.1; AT2G33610.
DR   GeneID; 817927; -.
DR   Gramene; AT2G33610.1; AT2G33610.1; AT2G33610.
DR   KEGG; ath:AT2G33610; -.
DR   Araport; AT2G33610; -.
DR   TAIR; locus:2051028; AT2G33610.
DR   eggNOG; KOG1279; Eukaryota.
DR   HOGENOM; CLU_004447_5_0_1; -.
DR   InParanoid; Q84JG2; -.
DR   OMA; EESPCTI; -.
DR   OrthoDB; 683891at2759; -.
DR   PhylomeDB; Q84JG2; -.
DR   PRO; PR:Q84JG2; -.
DR   Proteomes; UP000006548; Chromosome 2.
DR   ExpressionAtlas; Q84JG2; baseline and differential.
DR   Genevisible; Q84JG2; AT.
DR   GO; GO:0005634; C:nucleus; IDA:TAIR.
DR   GO; GO:0016514; C:SWI/SNF complex; ISS:TAIR.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006338; P:chromatin remodeling; ISS:TAIR.
DR   CDD; cd00167; SANT; 1.
DR   Gene3D; 1.10.10.10; -; 1.
DR   InterPro; IPR009057; Homeobox-like_sf.
DR   InterPro; IPR017930; Myb_dom.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   InterPro; IPR032451; SMARCC_C.
DR   InterPro; IPR007526; SWIRM.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   Pfam; PF00249; Myb_DNA-binding; 1.
DR   Pfam; PF04433; SWIRM; 1.
DR   Pfam; PF16495; SWIRM-assoc_1; 1.
DR   SMART; SM00717; SANT; 1.
DR   SUPFAM; SSF46689; SSF46689; 2.
DR   PROSITE; PS51293; SANT; 1.
DR   PROSITE; PS50934; SWIRM; 1.
PE   1: Evidence at protein level;
KW   Activator; Chromatin regulator; Coiled coil; Developmental protein;
KW   DNA-binding; Nucleus; Reference proteome; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..469
FT                   /note="SWI/SNF complex subunit SWI3B"
FT                   /id="PRO_0000344528"
FT   DOMAIN          48..145
FT                   /note="SWIRM"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00247"
FT   DOMAIN          223..274
FT                   /note="SANT"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   REGION          1..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          293..314
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          360..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          423..447
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        15..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        293..310
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        368..383
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   469 AA;  52411 MW;  BB4D35067B8520E1 CRC64;
     MAMKAPDPGG SGEILPSTPS LSETTSGGAA AASKSAQLPS SSSDIDNIHV PSYSSWFSWT
     DINDCEVRSL PEFFDSRSSS KNPKFYLYLR NSIIKQYRDD HPRKISFTDV RRTLVSDVVS
     IRRVFDFLDS WGLINYNSSA SAKPLKWEEK EAGKSAGDAA SEPATTVKET AKRNCNGCKA
     ICSIACFACD KYDLTLCARC YVRSNYRVGI NSSEFKRVEI SEESKPEWSD KEILLLLEAV
     MHYGDDWKKV ASHVIGRTEK DCVSQFVKLP FGEQFVKESD SEDGLEMFDQ IKDSDIPESE
     GIDKDGSSPN KRIKLTPLAD ASNPIMAQAA FLSALAGTNV AEAAARAAVR ALSDVDYEAD
     KNASRDPNRQ DANAASSGET TRNESERAWA DAKSLIEKEE HEVEGAIKET VEVEMKKIRD
     RIVHFEKLDL EMERSRKQLE EVRNLLFVDQ LNIFFHTRKA RKTEDRIEC
 
 
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